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Conserved domains on  [gi|380848751|ref|NP_001244160|]
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UDP-N-acetylglucosamine transferase subunit ALG13 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 144-273 1.12e-87

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


:

Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 277.46  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  144 MDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22795     1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  224 EIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYS 273
Cdd:cd22795    81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 410-489 2.29e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410518  Cd Length: 80  Bit Score: 171.96  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  410 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 489
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
PssE super family cl49515
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
4-49 5.99e-08

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


The actual alignment was detected with superfamily member NF041548:

Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 52.91  E-value: 5.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 380848751    4 GAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTC 49
Cdd:NF041548   67 GAGTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYD 112
 
Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 144-273 1.12e-87

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 277.46  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  144 MDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22795     1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  224 EIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYS 273
Cdd:cd22795    81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 410-489 2.29e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 171.96  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  410 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 489
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 161-268 7.02e-13

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 66.32  E-value: 7.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751   161 DASCLFRAISEQLFC-----SQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRD 235
Cdd:pfam02338    3 DGNCLYRSISHQLWGvhdvlRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 380848751   236 FILYR-------FPGKPPTYVTDNGYEDKILLCYSS-----SGHY 268
Cdd:pfam02338   83 IIVYKseggeelGGLKEYGIYLPLGWDPSLCLVYPRhlyylGGHY 127
PssE NF041548
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
4-49 5.99e-08

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 52.91  E-value: 5.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 380848751    4 GAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTC 49
Cdd:NF041548   67 GAGTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYD 112
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 4-42 9.97e-07

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 50.02  E-value: 9.97e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 380848751     4 GAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG 42
Cdd:pfam04101   80 GAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAG 118
 
Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 144-273 1.12e-87

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 277.46  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  144 MDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22795     1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  224 EIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYS 273
Cdd:cd22795    81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 144-272 4.35e-69

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 226.48  E-value: 4.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  144 MDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22794     1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 380848751  224 EIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVY 272
Cdd:cd22794    81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVY 129
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 144-273 4.96e-63

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438590 [Multi-domain]  Cd Length: 130  Bit Score: 209.71  E-value: 4.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  144 MDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22753     1 IDEYLDSLGLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  224 EIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYS 273
Cdd:cd22753    81 ELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGGNHYDSVYS 130
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 410-489 2.29e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 171.96  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  410 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 489
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 152-271 1.91e-29

OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438608 [Multi-domain]  Cd Length: 124  Bit Score: 113.80  E-value: 1.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  152 GLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEG--SFEKYLERLGDPKESAGQLEIRALS 229
Cdd:cd22771     1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDdeTFEDYVSRMREDGTWGGNLELQAAS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 380848751  230 LIYNRDFILYRFPGkpPTYVTDNGYEDK---ILLCYSSSGHYDSV 271
Cdd:cd22771    81 LVYRVNIVVHQLGQ--PRWEIENFPDKGartIHLSYHDGEHYNSV 123
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 158-271 7.71e-26

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 103.67  E-value: 7.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  158 TAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFES------YVEGSFEKYLERLGDPKESAGQLEIRALSLI 231
Cdd:cd22744     5 VPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPaeladeDDGEDFDEYLQRMRKPGTWGGELELQALANA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 380848751  232 YNRDFILY-RFPGKPPTYVTDNGYEDK---ILLCYSSSGHYDSV 271
Cdd:cd22744    85 LNVPIVVYsEDGGFLPVSVFGPGPGPSgrpIHLLYTGGNHYDAL 128
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 406-469 1.08e-22

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 92.25  E-value: 1.08e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380848751  406 DYMEYAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQ 469
Cdd:cd20448     1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 161-271 1.11e-22

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This subfamily includes bilaterial OTU domain-containing protein 3 (OTUD3), Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, and similar proteins. OTUD3 is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. OTU7 is a DUB that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438593 [Multi-domain]  Cd Length: 131  Bit Score: 94.55  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESY--------VEGSFEKYLERLGDPKESAGQLEIRALSLIY 232
Cdd:cd22756     8 DGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFseaatfaeDDEAFEDYLARMAKDGTYGDNLEIVAFARAY 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 380848751  233 NRDFILYRfPGkpPTYV------TDNGYEDKIL-LCYSSSGHYDSV 271
Cdd:cd22756    88 NVDVKVYQ-PD--PVYVisapedGSPGPARRVLhIAYHNWEHYSSV 130
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 414-467 4.54e-22

Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The TDRD13 family includes TDRD13 and OTU domain-containing protein 4 (OTUD4). TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410451  Cd Length: 54  Bit Score: 90.33  E-value: 4.54e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 380848751  414 QYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPV 467
Cdd:cd20380     1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVFVEELGEKKTVPYENLKPL 54
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 161-273 1.37e-19

OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU domain-containing protein 5 (OTUD5), also called deubiquitinating enzyme A (DUBA), is a phosphorylation-dependent deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can hydrolyze 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and may function as negative regulator of the innate immune system. It limits type I interferon production in macrophages and suppresses interleukin-17A production in T cells. OTUD5 also functions in an apoptotic signaling cascade by mediating the sequential activation of PDCD5 (programmed cell death 5) and p53 in response to genotoxic stress. In Drosophila, OTUD5/DUBA is essential for spermatogenesis. This subfamily also includes Arabidopsis thaliana OTU domain-containing protein 6, also called deubiquitinating enzyme OTU6 or otubain-like deubiquitinase 1 (OTLD1), which binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It also includes plant OTU6.


Pssm-ID: 438589 [Multi-domain]  Cd Length: 124  Bit Score: 85.68  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYR 240
Cdd:cd22752    10 DGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTEDFEEYINRKRQDGVWGNHIEIQAMSELYNRPIEVYA 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 380848751  241 FPGKP-PTYVTDNGYEDK-ILLCYSSSGHYDSVYS 273
Cdd:cd22752    90 YSTEPiNTFHEASSSDNEpIRLSYHGNSHYNSIVD 124
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 161-272 1.55e-19

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 85.55  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYR 240
Cdd:cd22796    13 DGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAMSEIYNRPIEVYS 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 380848751  241 FPGKPPTYVTDNGYEDK---ILLCYSSSGHYDSVY 272
Cdd:cd22796    93 YSNGEPINIFHGSYEGDdppIRLSYHDGNHYNSII 127
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 161-271 6.74e-18

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438585 [Multi-domain]  Cd Length: 144  Bit Score: 81.45  E-value: 6.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFC-----SQVHHLEIRKACVSYMRENQ---------QTFESYVEGSFEKYLERLGDPKESAGQLEIR 226
Cdd:cd22748    14 DGHCLYRAIADQLKLrggseEPYSYKELRKLAADYMRAHRddflpfltnDDGDLMTEEEFEEYCDKIENTAEWGGQLELR 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  227 ALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLC-----YSSSGHYDSV 271
Cdd:cd22748    94 ALSKALKRPIHVYQAGSPPLVIGEEFDSGEPLRLSyhrhaYGLGEHYNSV 143
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 145-272 1.99e-17

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438588 [Multi-domain]  Cd Length: 134  Bit Score: 79.51  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  145 DEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQ-TFESYVEGSFEKYLERLGDPKESAGQL 223
Cdd:cd22751     2 LRRLDLYGLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPElYYEFYVPEEYDEYLKKMSKDGEWGDEL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 380848751  224 EIRALSLIYN-RDFILYRFPGKPP-TYVTDNGYEDK--ILLCYSSSGHYDSVY 272
Cdd:cd22751    82 TLQAAADAFGvKIHVITSFEDNWFlEIEPRGLVRSKrvLFLSYWAEVHYNSIY 134
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 161-271 2.60e-16

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 76.54  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLF--CSQVHHLEIRKACVSYMRENQQTFESYV------EGSFEKYLERLGDPKESAGQLEIRALSLIY 232
Cdd:cd22758    14 DGNCFFHAVSDQLYgnGIEHSHKELRQQAVNYLRENPELYDGFFlsefdeEESWEEYLNRMSKDGTWGDHIILQAAANLF 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 380848751  233 NRDF-ILYRFPGKPPTYVTDNGYEDK--ILLCYSSSGHYDSV 271
Cdd:cd22758    94 NVRIvIISSDGSDETTIIEPGNSKNGrtIYLGHIGENHYVSL 135
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 161-272 2.71e-14

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438594 [Multi-domain]  Cd Length: 128  Bit Score: 70.70  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYV---EGSFEK----YLERLGDPKESAGQLEIRALSLIYN 233
Cdd:cd22757     9 DGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYThdsEGNNYKsaeeYRADMSKPGTYGTLCELVAAAELYP 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 380848751  234 RDFILYRfPGKPPTYVTDNGYEDKILLCYS--SSGHYDsVY 272
Cdd:cd22757    89 FHFEVYR-NGKLYASFGDPSNPVKRLKFSGdlSNGHFD-VL 127
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 140-271 1.42e-13

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 68.85  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  140 NEASMDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEG--SFEKYLERLGDPK 217
Cdd:cd22770     1 NFVSFANQLQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDdvPFDKHVANLSKPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 380848751  218 ESAGQLEIRALSLIYNRDFILYRfPGKPPTYV--TDNGYEDKILLCYSSSGHYDSV 271
Cdd:cd22770    81 TYAGNDAIVAFARLHQVNVVIHQ-LNAPLWQIrgTEKSSSRELHISYHNGDHYSSV 135
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 161-268 7.02e-13

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 66.32  E-value: 7.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751   161 DASCLFRAISEQLFC-----SQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRD 235
Cdd:pfam02338    3 DGNCLYRSISHQLWGvhdvlRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 380848751   236 FILYR-------FPGKPPTYVTDNGYEDKILLCYSS-----SGHY 268
Cdd:pfam02338   83 IIVYKseggeelGGLKEYGIYLPLGWDPSLCLVYPRhlyylGGHY 127
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 161-271 1.56e-12

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 65.74  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYV---EGSFEKYLERLGDPKES--AGQLEIRALS------ 229
Cdd:cd22755     9 DGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLrsdYESVEEYLEKSRMRYDGtwATDVEIFAAAtllgvd 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 380848751  230 -LIYNRDF---ILYRFPGKPPTYVTDNGYedkILLCYSSSGHYDSV 271
Cdd:cd22755    89 iYVYSKGGykwLLYSPRFKLGKRNGSREA---IYLKNTNGNHFEPV 131
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
 148-271 3.05e-12

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 65.44  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  148 LGSLGLFRKLTAKDASCLFRAISEQL-----FCSQVHHLEIRKACVSYMRENQQTFESYVEG---------SFEKYLERL 213
Cdd:cd22797     5 LAPLGLAIKEIKADGHCLYRAVEDQLqlrggGAPAPDYQQLRELAADYMRAHPDDFLPFLEDedeggdgdeAFEAYCREV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380848751  214 GDPKESAGQLEIRALSLIYNRDFILYrfPGKPPTYVTDNGYED---KILLCYSSSG-----HYDSV 271
Cdd:cd22797    85 ESTAAWGGQLELGALAHALRRHIKVY--SAGMPDVEMGEEYAGtgpPLRLCYHRHAfglgeHYNSV 148
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 161-272 4.71e-12

OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; This subfamily includes Schizosaccharomyces pombe and Saccharomyces cerevisiae OTU domain-containing protein 2 (OTU2) and similar proteins. S. pombe OTU2 is a ubiquitin thioesterase/hydrolase (EC 3.4.19.12) that can remove conjugated ubiquitin from protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Fungal OTU2 bbelongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438599 [Multi-domain]  Cd Length: 142  Bit Score: 64.56  E-value: 4.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLfcsQVHHL-------EIRKACVSYMRENQQTFESYV------EGSFEKYLERLGDPKESAGQLEIRA 227
Cdd:cd22762    15 DGHCLFAAIADQL---QLRGSeinldykELRKLAAEYIRKHPDDFEPFLfeetdeLEDIDEYCKKIENTAEWGGELELLA 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 380848751  228 LSLIYNRDFILYRFPGkPPTYVTDNGYEDKILLC-------YSSSGHYDSVY 272
Cdd:cd22762    92 LAKAFGVPIHVVQAEG-RVIKINEEGDSDKPELWlayykhsYGLGEHYNSLR 142
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 145-272 5.32e-12

OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU domain-containing protein 1 (OTUD1), also called DUBA-7 in humans, is a deubiquitinating enzyme/ubiquitinyl hydrolase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin; this specificity is facilitated by the C-terminal Ub-interacting motif (UIM) of OTUD1. It interacts and promotes the deubiquitination of myeloid cell leukemia 1 (MCL1), a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumorigenesis. OTUD1 also deubiquitinates IFN regulatory factor 3 (IRF3) and attenuates its function; IRF3 is critical for the transcription of type I IFNs in defensing virus and promoting inflammatory responses. Loss-of-function mutations of OTUD1 associated with multiple autoimmune diseases including systemic lupus erythematosus (SLE), rheumatoid arthritis (RA), ulcerative colitis (UC) and Hashimoto's thyroiditis (HT). OTUD1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438584 [Multi-domain]  Cd Length: 149  Bit Score: 64.83  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  145 DEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLE 224
Cdd:cd22747    13 DKYLRERNKYRFHIIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIEGDVGEFLIKAAQDGAWAGYPE 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 380848751  225 IRALSLIYNRDFILYR--FPGKP--PTYVTDNGYED----KILLCYSSSGHYDSVY 272
Cdd:cd22747    93 LLAMGQMLNVNIRLTTggSLESPtvSTMVHYLGPEDsgkpSIWLSWLSNGHYDAVF 148
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 146-271 5.90e-11

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 61.36  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  146 EYLGSLGLFRKLTAKDASCLFRAISEQLfcsQVHHLEI-----RKACVSYMRENQQTF----------ESYVEGSFEKYL 210
Cdd:cd22761     3 KILKERGLKIHEIPSDGDCLYNAIAHQL---SLRGIETsveelRKQTADYMRENKDDFlpfltnpdtgDPLTEEEFEKYC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380848751  211 ERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYS----SSG-HYDSV 271
Cdd:cd22761    80 DDVENTGAWGGQLELRALSHVLKRPIEVIQAEGPPIIIGEEFKSGKPLILTYHrhayGLGeHYNSV 145
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
 161-269 1.11e-08

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU3 and OTU4 may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 54.97  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQ-----VHHLE------IRKACVSYMRENQQTFES---YVEGSFEKYLERLGDPKESAGQLEIR 226
Cdd:cd22746    10 DGRCLFRAVARGLALATggrplSERREradadaLRKAVVEEIRKRRDELFEgslVIEGDFDAYCQRMSHPDTWGGEPELL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 380848751  227 ALSLIYNRDFILYRFPGKPP------TYVTDNGYEDKILLCYSSSGHYD 269
Cdd:cd22746    90 MLADVLQRPIAVYLPTPGKGglrkiqEYGEEYLGGEPIRLLYNGGNHYD 138
PssE NF041548
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
4-49 5.99e-08

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 52.91  E-value: 5.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 380848751    4 GAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTC 49
Cdd:NF041548   67 GAGTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYD 112
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 4-42 9.97e-07

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 50.02  E-value: 9.97e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 380848751     4 GAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG 42
Cdd:pfam04101   80 GAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAG 118
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 418-467 1.21e-06

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 46.09  E-value: 1.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  418 GDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPV 467
Cdd:cd21182     1 GDKCLAPYSDDGKYYEATIEEITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 417-466 9.75e-06

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 43.66  E-value: 9.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 380848751  417 LGDKCQVCLESEGRYYNAHIQEVgNENNSVTVFIEELAEKHVVPLANLKP 466
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEV-LSNDKVEVFFVDYGNTETVPLSDLRP 49
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 417-468 3.03e-05

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Overexpression of SPF30 causes apoptosis. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 42.29  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 380848751  417 LGDKCQVCLESEGRYYNAHIQEVGnENNSVTVFIEELAEKHVVPLANLKPVT 468
Cdd:cd20399     3 VGDKCMAVWSEDGQYYEATIEEIS-EDGTCTVTFDGYGNTEVTPLSQLKPRE 53
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
 158-270 1.91e-04

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; Deubiquitinating enzyme OTU4, also called OTU domain-containing protein 4, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU4 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438597 [Multi-domain]  Cd Length: 138  Bit Score: 42.75  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  158 TAKDASCLFRAIS---------------EQLFCSQvhhlEIR-KACVSYMRENQQTfESYVEGSFEKYLERLGDPKESAG 221
Cdd:cd22760     7 IAGDGRCLFRAVAhgeclargkaapdeeRERELAD----ELRtRAADELVKRREET-EWFIEGDFDEYVARMRRPGVWGG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 380848751  222 QLEIRALSLIYNRDFILY-RFPGKPP-----TYVTDNGYEDKILLCYSSSGHYDS 270
Cdd:cd22760    82 EPELLMLSHVLQRPITVYmADEGEGGlisiaEYGQEYGKGNPIRVLFHGFGHYEA 136
OTU_plant_OTU1_2-like cd22793
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar ...
 155-269 2.48e-04

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar proteins; Deubiquitinating enzyme OTU2, also called OTU domain-containing protein 2, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU2 exhibited equivalent binding affinities for K48- and K63-linked ubiquitin chains and no cleavage activity toward linear UB chains. It may also be involved in endoplasmic-reticulum-associated protein degradation (ERAD). OTU2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438614  Cd Length: 163  Bit Score: 42.70  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  155 RKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTF-ESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYN 233
Cdd:cd22793     5 RRVIDSDNSCLFNAVGYVMEGSRKKAPELRQVIADAVLSDPFEYnEAFLGKSNKEYCEWILNPNSWGGAIELSILSDHYG 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380848751  234 RDFILYRF-PGKPPTYVTDNGYEDKILLCYssSG-HYD 269
Cdd:cd22793    85 REIAAFDIqTKRCDVYGEGKGYTERVMLIY--DGlHYD 120
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
 161-272 4.00e-04

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


Pssm-ID: 438582  Cd Length: 161  Bit Score: 42.09  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQV-HHLEIRKACVSYMRENQQTFESYVEG-SFEKYLERLGDPKESAGQLEIRALSLIYN----- 233
Cdd:cd22745    11 DNSCLFTSISYLLEGGLLdSAPELREIVADAILSDPDTYNEAILGkPPDEYCAWILKPDSWGGAIELSILSKHFGveicv 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 380848751  234 ---RDFILYRFpGKpptyvtDNGYEDKILLCYssSG-HYDSVY 272
Cdd:cd22745    91 vdvQTGRVDRF-GE------DKGYSKRIFLLY--SGiHYDALA 124
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
 161-233 8.94e-04

OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438580  Cd Length: 148  Bit Score: 40.66  E-value: 8.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVE--GSFEKYLERLGDPKESAGQLEIRALSLIYN 233
Cdd:cd21880    30 DGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLyyLSLEEYLRDAMKDGYWGGSLEAEILSKALG 104
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
 161-229 1.25e-03

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.


Pssm-ID: 438612  Cd Length: 137  Bit Score: 40.28  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380848751  161 DASCLFRAISEQLFCSQVHHLEIRKACVSYMRENqqtfESYVEGSFEKYLERLGDPKESAGQLEIRALS 229
Cdd:cd22791     9 DGNCLFRAASLLLFGDESLHLELRLRTVLELVLN----SEFYEAIYEAEIKATCKPGSYSGIWHIYALS 73
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
 161-269 5.11e-03

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; Deubiquitinating enzyme OTU3, also called OTU domain-containing protein 3, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU3 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU3 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438596  Cd Length: 159  Bit Score: 38.86  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380848751  161 DASCLFRAISEQLFCSQVHHL----------EIRKA-----CVSYMRENQQTFESY---VEGSFEKYLERLGDPKESAGQ 222
Cdd:cd22759    11 DGRCMFRALVKGLAANKGIFLsgreeeqeadELRLAvaealCRSEERRRDYEEALIaitVEGSLDRYCRRIQRPDFWGGE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380848751  223 LEIRALSLIYNRDFILY------RFPGKPPTYVTDNGYEDKIL-------------LCYSSSGHYD 269
Cdd:cd22759    91 SELLVLSKMLKQPIIVYipeseaKNGGWGSGFIPIQKYGEEFAkgtkgrkgrkpvrLLYSGSNHYD 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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